ENDOR characterization of an iron-alkene complex provides insight into a corresponding organometallic intermediate of nitrogenase.

ABSTRACT: A bio-organometallic intermediate, denoted PA, was previously trapped during the reduction of propargyl alcohol to allyl alcohol (AA) by nitrogenase, and a similar one was trapped during acetylene reduction, representing foundational examples of alkene binding to a metal center in biology. ENDOR spectroscopy led to the conclusion that these intermediates have η² binding of the alkene, with the hydrogens on the terminal carbon structurally/magnetically equivalent and related by local mirror symmetry. However, our understanding of both the PA intermediate, and of the dependability of the ENDOR analysis on which this understanding was based, was constrained by the absence of reference iron-alkene complexes for EPR/ENDOR comparison. Here, we report an ENDOR stud

SUBMITTER: Horitani M 

PROVIDER: S-EPMC5620524 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature